ID A0A0R2U0K6_9ACTN Unreviewed; 345 AA.
AC A0A0R2U0K6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=3-isopropylmalate dehydrogenase {ECO:0000313|EMBL:KRO92790.1};
DE EC=1.1.1.85 {ECO:0000313|EMBL:KRO92790.1};
GN ORFNames=ABS08_06980 {ECO:0000313|EMBL:KRO92790.1};
OS Actinobacteria bacterium BACL4 MAG-120507-bin0.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1655610 {ECO:0000313|EMBL:KRO92790.1, ECO:0000313|Proteomes:UP000051564};
RN [1] {ECO:0000313|EMBL:KRO92790.1, ECO:0000313|Proteomes:UP000051564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL1 MAG-120507-bin0 {ECO:0000313|EMBL:KRO92790.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate
CC + CO2 + NADH; Xref=Rhea:RHEA:32271, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17865, ChEBI:CHEBI:35121, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.1.1.85;
CC Evidence={ECO:0000256|ARBA:ARBA00000624};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRO92790.1}.
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DR EMBL; LICQ01000029; KRO92790.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2U0K6; -.
DR Proteomes; UP000051564; Unassembled WGS sequence.
DR GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR PANTHER; PTHR43275; D-MALATE DEHYDROGENASE [DECARBOXYLATING]; 1.
DR PANTHER; PTHR43275:SF1; D-MALATE DEHYDROGENASE [DECARBOXYLATING]; 1.
DR Pfam; PF00180; Iso_dh; 1.
DR SMART; SM01329; Iso_dh; 1.
DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR PROSITE; PS00470; IDH_IMDH; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022430};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Oxidoreductase {ECO:0000313|EMBL:KRO92790.1}.
FT DOMAIN 5..340
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 345 AA; 37117 MW; 6EDF616637D4A146 CRC64;
MKNFNLAVIA GDGIGPEVVT EGLRVLDTVA KKYDLNFSKT NYELGAAYWH KTGETLPDSV
MAELAKADVI LLGAVGDPSV PSGVLERGLL LKLRFAFEHY INLRPAKLFP GVTSPITNNK
GIDFVVVREG TEGLYVGAGS IKDEGTNKEL AIEESINTYK GVERVIRDAF NRAQSRPRKK
LTLVHKNNVL TRAGGLWSRV FKEVAKDFTD VTTDYLHVDA ASMFFVTNPE RFDVVVTDNL
FGDIITDIAA AICGGIGLAA SGNINPTGEF PSMFEPVHGS APDIAGKNQA DPTATVLSVA
MMLNHLGQTQ AAKDVENAVA QDLLNRGDKK RSTTEIGDAL VRGVA
//
